메뉴 건너뛰기




Volumn 109, Issue 19, 2012, Pages 7469-7474

Crystal structure of a Trypanosoma brucei metacaspase

Author keywords

Apoptosis; Clan CD; Parasite; X ray crystallography

Indexed keywords

ARGININE; ASPARTIC ACID; CASPASE; METACASPASE 2; MONOMER; UNCLASSIFIED DRUG;

EID: 84860798287     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1200885109     Document Type: Article
Times cited : (75)

References (40)
  • 1
    • 10644282148 scopus 로고    scopus 로고
    • The protein structures that shape caspase activity, specificity, activation and inhibition
    • DOI 10.1042/BJ20041142
    • Fuentes-Prior P, Salvesen GS (2004) The protein structures that shape caspase activity, specificity, activation and inhibition. Biochem J 384:201-232. (Pubitemid 39656233)
    • (2004) Biochemical Journal , vol.384 , Issue.2 , pp. 201-232
    • Fuentes-Prior, P.1    Salvesen, G.S.2
  • 3
    • 84855266765 scopus 로고    scopus 로고
    • The meaning of death: Evolution and ecology of apoptosis in protozoan parasites
    • Reece SE, Pollitt LC, Colegrave N, Gardner A (2011) The meaning of death: Evolution and ecology of apoptosis in protozoan parasites. PLoS Pathog 7:e1002320.
    • (2011) PLoS Pathog , vol.7
    • Reece, S.E.1    Pollitt, L.C.2    Colegrave, N.3    Gardner, A.4
  • 4
    • 0033638182 scopus 로고    scopus 로고
    • Identification of paracaspases and metacaspases: Two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma
    • Uren AG, et al. (2000) Identification of paracaspases and metacaspases: Two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma. Mol Cell 6:961-967.
    • (2000) Mol Cell , vol.6 , pp. 961-967
    • Uren, A.G.1
  • 7
    • 78649707971 scopus 로고    scopus 로고
    • Arabidopsis type I metacaspases control cell death
    • Coll NS, et al. (2010) Arabidopsis type I metacaspases control cell death. Science 330: 1393-1397.
    • (2010) Science , vol.330 , pp. 1393-1397
    • Coll, N.S.1
  • 9
    • 78650231796 scopus 로고    scopus 로고
    • Processing of metacaspase into a cytoplasmic catalytic domain mediating cell death in Leishmania major
    • Zalila H, et al. (2011) Processing of metacaspase into a cytoplasmic catalytic domain mediating cell death in Leishmania major. Mol Microbiol 79:222-239.
    • (2011) Mol Microbiol , vol.79 , pp. 222-239
    • Zalila, H.1
  • 11
    • 79960216439 scopus 로고    scopus 로고
    • Metacaspases
    • Tsiatsiani L, et al. (2011) Metacaspases. Cell Death Differ 18:1279-1288.
    • (2011) Cell Death Differ , vol.18 , pp. 1279-1288
    • Tsiatsiani, L.1
  • 13
    • 17644412048 scopus 로고    scopus 로고
    • Two Arabidopsis metacaspases AtMCP1b and AtMCP2b are arginine/lysine- specific cysteine proteases and activate apoptosis-like cell death in yeast
    • DOI 10.1074/jbc.M413527200
    • Watanabe N, Lam E (2005) Two Arabidopsis metacaspases AtMCP1b and AtMCP2b are arginine/lysine-specific cysteine proteases and activate apoptosis-like cell death in yeast. J Biol Chem 280:14691-14699. (Pubitemid 40562816)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.15 , pp. 14691-14699
    • Watanabe, N.1    Lam, E.2
  • 14
    • 36549073184 scopus 로고    scopus 로고
    • Metacaspase 2 of Trypanosoma brucei is a calcium-dependent cysteine peptidase active without processing
    • DOI 10.1016/j.febslet.2007.11.009, PII S0014579307011441
    • Moss CX, Westrop GD, Juliano L, Coombs GH, Mottram JC (2007) Metacaspase 2 of Trypanosoma brucei is a calcium-dependent cysteine peptidase active without processing. FEBS Lett 581:5635-5639. (Pubitemid 350179768)
    • (2007) FEBS Letters , vol.581 , Issue.29 , pp. 5635-5639
    • Moss, C.X.1    Westrop, G.D.2    Juliano, L.3    Coombs, G.H.4    Mottram, J.C.5
  • 15
    • 79953208949 scopus 로고    scopus 로고
    • Calcium-dependent activation and autolysis of Arabidopsis metacaspase 2d
    • Watanabe N, Lam E (2011) Calcium-dependent activation and autolysis of Arabidopsis metacaspase 2d. J Biol Chem 286:10027-10040.
    • (2011) J Biol Chem , vol.286 , pp. 10027-10040
    • Watanabe, N.1    Lam, E.2
  • 16
    • 70449529844 scopus 로고    scopus 로고
    • Tudor staphylococcal nuclease is an evolutionarily conserved component of the programmed cell death degradome
    • Sundström JF, et al. (2009) Tudor staphylococcal nuclease is an evolutionarily conserved component of the programmed cell death degradome. Nat Cell Biol 11: 1347-1354.
    • (2009) Nat Cell Biol , vol.11 , pp. 1347-1354
    • Sundström, J.F.1
  • 17
    • 51849114272 scopus 로고    scopus 로고
    • A non-death role of the yeast metacaspase: Yca1p alters cell cycle dynamics
    • Lee RE, Puente LG, Kaern M, Megeney LA (2008) A non-death role of the yeast metacaspase: Yca1p alters cell cycle dynamics. PLoS ONE 3:e2956.
    • (2008) PLoS ONE , vol.3
    • Lee, R.E.1    Puente, L.G.2    Kaern, M.3    Megeney, L.A.4
  • 18
    • 77955791979 scopus 로고    scopus 로고
    • Metacaspase Yca1 is required for clearance of insoluble protein aggregates
    • Lee RE, Brunette S, Puente LG, Megeney LA (2010) Metacaspase Yca1 is required for clearance of insoluble protein aggregates. Proc Natl Acad Sci USA 107:13348-13353.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 13348-13353
    • Lee, R.E.1    Brunette, S.2    Puente, L.G.3    Megeney, L.A.4
  • 19
    • 37349064941 scopus 로고    scopus 로고
    • An essential role for the Leishmania major metacaspase in cell cycle progression
    • DOI 10.1038/sj.cdd.4402232, PII 4402232, Special issue on Tumor stress, cell death and the ensuing immune response
    • Ambit A, Fasel N, Coombs GH, Mottram JC (2008) An essential role for the Leishmania major metacaspase in cell cycle progression. Cell Death Differ 15:113-122. (Pubitemid 350286179)
    • (2008) Cell Death and Differentiation , vol.15 , Issue.1 , pp. 113-122
    • Ambit, A.1    Fasel, N.2    Coombs, G.H.3    Mottram, J.C.4
  • 21
    • 0036499652 scopus 로고    scopus 로고
    • Classification of the caspase-hemoglobinase fold: Detection of new families and implications for the origin of the eukaryotic separins
    • DOI 10.1002/prot.10060
    • Aravind L, Koonin EV (2002) Classification of the caspase-hemoglobinase fold: Detection of new families and implications for the origin of the eukaryotic separins. Proteins 46:355-367. (Pubitemid 34184587)
    • (2002) Proteins: Structure, Function and Genetics , vol.46 , Issue.4 , pp. 355-367
    • Aravind, L.1    Koonin, E.V.2
  • 22
    • 84862907834 scopus 로고    scopus 로고
    • Crystal structure of the mucosa-associated lymphoid tissue lymphoma translocation 1 (MALT1) paracaspase region
    • Yu JW, Jeffrey PD, Ha JY, Yang X, Shi Y (2011) Crystal structure of the mucosa-associated lymphoid tissue lymphoma translocation 1 (MALT1) paracaspase region. Proc Natl Acad Sci USA 108:21004-21009.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 21004-21009
    • Yu, J.W.1    Jeffrey, P.D.2    Ha, J.Y.3    Yang, X.4    Shi, Y.5
  • 24
    • 53749083462 scopus 로고    scopus 로고
    • Small molecule-induced allosteric activation of the Vibrio cholerae RTX cysteine protease domain
    • Lupardus PJ, Shen A, Bogyo M, Garcia KC (2008) Small molecule-induced allosteric activation of the Vibrio cholerae RTX cysteine protease domain. Science 322:265-268.
    • (2008) Science , vol.322 , pp. 265-268
    • Lupardus, P.J.1    Shen, A.2    Bogyo, M.3    Garcia, K.C.4
  • 27
    • 0037384483 scopus 로고    scopus 로고
    • Clan CD cysteine peptidases of parasitic protozoa
    • DOI 10.1016/S1471-4922(03)00038-2
    • Mottram JC, Helms MJ, Coombs GH, Sajid M (2003) Clan CD cysteine peptidases of parasitic protozoa. Trends Parasitol 19(4):182-187. (Pubitemid 36411975)
    • (2003) Trends in Parasitology , vol.19 , Issue.4 , pp. 182-187
    • Mottram, J.C.1    Helms, M.J.2    Coombs, G.H.3    Sajid, M.4
  • 28
    • 33645742663 scopus 로고    scopus 로고
    • Bloodstream form Trypanosoma brucei depend upon multiple metacaspases associated with RAB11-positive endosomes
    • Helms MJ, et al. (2006) Bloodstream form Trypanosoma brucei depend upon multiple metacaspases associated with RAB11-positive endosomes. J Cell Sci 119:1105-1117.
    • (2006) J Cell Sci , vol.119 , pp. 1105-1117
    • Helms, M.J.1
  • 29
    • 81155154312 scopus 로고    scopus 로고
    • Trypanosoma brucei metacaspase 4 is a pseudopeptidase and a virulence factor
    • Proto WR, et al. (2011) Trypanosoma brucei metacaspase 4 is a pseudopeptidase and a virulence factor. J Biol Chem 286:39914-39925.
    • (2011) J Biol Chem , vol.286 , pp. 39914-39925
    • Proto, W.R.1
  • 30
    • 0034674168 scopus 로고    scopus 로고
    • The anatomy of protein beta-sheet topology
    • Zhang C, Kim SH (2000) The anatomy of protein beta-sheet topology. J Mol Biol 299: 1075-1089.
    • (2000) J Mol Biol , vol.299 , pp. 1075-1089
    • Zhang, C.1    Kim, S.H.2
  • 31
    • 2942746419 scopus 로고    scopus 로고
    • Caspase activation: Revisiting the induced proximity model
    • Shi YG (2004) Caspase activation: Revisiting the induced proximity model. Cell 117: 855-858.
    • (2004) Cell , vol.117 , pp. 855-858
    • Shi, Y.G.1
  • 32
    • 67650290548 scopus 로고    scopus 로고
    • Mechanistic and structural insights into the proteolytic activation of Vibrio cholerae MARTX toxin
    • Shen A, et al. (2009) Mechanistic and structural insights into the proteolytic activation of Vibrio cholerae MARTX toxin. Nat Chem Biol 5:469-478.
    • (2009) Nat Chem Biol , vol.5 , pp. 469-478
    • Shen, A.1
  • 35
    • 0031554904 scopus 로고    scopus 로고
    • Crystal structure of the wild-type human procathepsin B at 2.5 A resolution reveals the native active site of a papain-like cysteine protease zymogen
    • DOI 10.1006/jmbi.1997.1218
    • Podobnik M, Kuhelj R, Turk V, Turk D (1997) Crystal structure of the wild-type human procathepsin B at 2.5 A resolution reveals the native active site of a papain-like cysteine protease zymogen. J Mol Biol 271:774-788. (Pubitemid 27376053)
    • (1997) Journal of Molecular Biology , vol.271 , Issue.5 , pp. 774-788
    • Podobnik, M.1    Kuhelj, R.2    Turk, V.3    Turk, D.4
  • 36
    • 79151469464 scopus 로고    scopus 로고
    • Substrate-induced conformational changes occur in all cleaved forms of caspase-6
    • Vaidya S, Velázquez-Delgado EM, Abbruzzese G, Hardy JA (2011) Substrate-induced conformational changes occur in all cleaved forms of caspase-6. J Mol Biol 406:75-91.
    • (2011) J Mol Biol , vol.406 , pp. 75-91
    • Vaidya, S.1    Velázquez-Delgado, E.M.2    Abbruzzese, G.3    Hardy, J.A.4
  • 38
    • 0018695554 scopus 로고
    • Lanthanides as probes for calcium in biological systems
    • Martin RB, Richardson FS (1979) Lanthanides as probes for calcium in biological systems. Q Rev Biophys 12(2):181-209. (Pubitemid 10241609)
    • (1979) Quarterly Reviews of Biophysics , vol.12 , Issue.2 , pp. 181-209
    • Martin, R.B.1    Richardson, F.S.2
  • 39
    • 79953883005 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced apoptosis in Leishmania through Ca2+-dependent and caspase-independent mechanism
    • Dolai S, Pal S, Yadav RK, Adak S (2011) Endoplasmic reticulum stress-induced apoptosis in Leishmania through Ca2+-dependent and caspase-independent mechanism. J Biol Chem 286:13638-13646.
    • (2011) J Biol Chem , vol.286 , pp. 13638-13646
    • Dolai, S.1    Pal, S.2    Yadav, R.K.3    Adak, S.4
  • 40
    • 77649190040 scopus 로고    scopus 로고
    • Design and evaluation of Trypanosoma brucei metacaspase inhibitors
    • Berg M, et al. (2010) Design and evaluation of Trypanosoma brucei metacaspase inhibitors. Bioorg Med Chem Lett 20:2001-2006.
    • (2010) Bioorg Med Chem Lett , vol.20 , pp. 2001-2006
    • Berg, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.